ID   KPRS4_SPIOL             Reviewed;         318 AA.
AC   Q9XGA1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase 4;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase 4;
GN   Name=PRS4;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=9952445; DOI=10.1104/pp.119.2.497;
RA   Krath B.N., Hove-Jensen B.;
RT   "Organellar and cytosolic localization of four phosphoribosyl diphosphate
RT   synthase isozymes in spinach.";
RL   Plant Physiol. 119:497-506(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC         diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:456215; EC=2.7.6.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ006943; CAB43602.1; -; mRNA.
DR   AlphaFoldDB; Q9XGA1; -.
DR   SMR; Q9XGA1; -.
DR   PRIDE; Q9XGA1; -.
DR   SABIO-RK; Q9XGA1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   PANTHER; PTHR10210; PTHR10210; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; SSF53271; 2.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN           1..318
FT                   /note="Ribose-phosphate pyrophosphokinase 4"
FT                   /id="PRO_0000141102"
FT   REGION          222..237
FT                   /note="Binding of phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255"
FT   BINDING         139
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  35385 MW;  1B493F769430025C CRC64;
     MEKPNTKQVL LFYCVEAEEL ARKVAAQSPL ITLQSINWRS FDDGFPNLFI NNAQDIRGQH
     VAFLAAFSSP AVIFEQLSVI YALPRLFVAS FTLVLPFFPT GSFERMEEEG DVATAFTMAR
     ILSNIPVSRG GPTSVVIYDI HALQERFYFS DNVLPLFETG IPLLKQRLDQ LPDADKIVVA
     FPDDGAWKRF HKQLDHFPMV VCAKVREGDK RIVRLKEGNP AGCHVVIVDD LVQSGGTLIE
     CQKVLAAHGA TKVSAYVTHA VFPKNSFERF THKDDGSDKA FTYFWITDSC PRTVKSIANK
     APFEVLSLAG SIADALQI